Comparative studies on the structure of the light chains of human immunoglobulins. IV. Assignment of a subsubgroup.:IV. Assignment of a Subsubgroup

J-STAGE
  • KAMETANI Fuyuki
    Department of Chemistry, Faculty of Science, Tokyo Metropolitan University
  • TAKAYASU Tatsunori
    Department of Chemistry, Faculty of Science, Tokyo Metropolitan University
  • SUZUKI Satoru
    Department of Chemistry, Faculty of Science, Tokyo Metropolitan University
  • SHINODA Tomotaka
    Department of Chemistry, Faculty of Science, Tokyo Metropolitan University
  • OKUYAMA Tsuneo
    Department of Chemistry, Faculty of Science, Tokyo Metropolitan University
  • SHIMIZU Akira
    Osaka Medical Center and Research Institute for Maternal and Child Health

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Description

Amino acid sequence analysis was done on a human J. Bence Jones protein NIG-64 with the major objective of determining the sequence of the variable region. Nineteen tryptic peptides covering 216 residues were isolated from the completely reduced and aminoethylated protein, and 17 of these were completely sequenced. These comprised the entire variable region and 11 from the constant region. For the remaining peptides covering the rest of the constant region, only partial sequences or the amino acid compositions were determined. All the tryptic peptides could be arranged in order on the basis of the above results and homology with other human λ light chains of the same isotype. The sequence of the variable region of the protein is highly homologous with that of protein New of subgroup VλI as compared with other proteins of the same subgroup, suggesting that subgroup VλI may be further divided into subsubgroups, namely subsubgroups VλI-1 and VλI-2.

Journal

  • J Biochem (Tokyo)

    J Biochem (Tokyo) 93 (2), 421-429, 1983

    The Japanese Biochemical Society

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